Evidence for additional subunits associated to the mouse interleukin 2 receptor p55/p75 complex.
Previous studies have indicated that high-affinity interleukin 2 receptors (IL-2R) are comprised of at least two distinct noncovalently associated subunits of Mr 55,000 (p55) and Mr 75,000 (p75). To biochemically characterize p75, we have directly isolated IL-2R using affinity precipitations with immobilized IL-2. We now report that at least some mouse p75 appears to exist as a disulfide-linked heterodimer with a subunit of Mr 22,000 (p22). These findings suggest that functional high-affinity mouse IL-2R may be comprised of at least three distinct subunits. The possibility of an even more complex structure is suggested by the coprecipitation of a protein of Mr 40,000-45,000 (p40) that may represent an additional IL-2R-associated protein.
Saragovi
H
H
Department of Microbiology and Immunology, University of Miami School of Medicine, FL 33101.
Malek
T R
TR
D000818:Animals; D000911:Antibodies, Monoclonal; D002460:Cell Line; D002462:Cell Membrane / Q000276:immunology; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007376:Interleukin-2 / Q000378:metabolism; D046911:Macromolecular Substances; D051379:Mice; D008954:Models, Biological; D008970:Molecular Weight; D015375:Receptors, Interleukin-2 / Q000302:isolation & purification* / Q000378:metabolism; D013601:T-Lymphocytes / Q000276:immunology
D000911:Antibodies, Monoclonal; D007376:Interleukin-2; D046911:Macromolecular Substances; D015375:Receptors, Interleukin-2